Linked Life Data

21421309

Source:http://linkedlifedata.com/resource/pubmed/id/21421309

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2011-4-22
pubmed:abstractText
The celB gene of Caldicellulosiruptor saccharolyticus was cloned and expressed in Escherichia coli to create a recombinant biocatalyst for hydrolyzing lignocellulosic biomass at high temperature. The GH5 domain of CelB hydrolyzed 4-nitrophenyl-?-D-cellobioside and carboxymethyl cellulose with optimum activity at pH 4.7-5.5 and 80°C. The recombinant GH5 and CBM3-GH5 constructs were both stable at 80°C with half-lives of 23 h and 39 h, respectively, and retained >94% activity after 48 h at 70°C. Enzymatic hydrolysis of corn stover and cellulose pretreated with the ionic liquid 1-ethyl-3-methylimidazolium acetate showed that GH5 and CBM3-GH5 primarily produce cellobiose, with product yields for CBM3-GH5 being 1.2- to 2-fold higher than those for GH5. Confocal microscopy of bound protein on cellulose confirmed tighter binding of CBM3-GH5 to cellulose than GH5, indicating that the enhancement of enzymatic activity on solid substrates may be due to the substrate binding activity of CBM3 domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1873-2976
pubmed:author
pubmed:copyrightInfo
Published by Elsevier Ltd.
pubmed:issnType
Electronic
pubmed:volume
102
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5988-94
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Enzymatic hydrolysis of cellulose by the cellobiohydrolase domain of CelB from the hyperthermophilic bacterium Caldicellulosiruptor saccharolyticus.
pubmed:affiliation
Deconstruction Division, Joint BioEnergy Institute, Emeryville, CA 94608, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.